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Database: UniProt
Entry: A0A091AR36_9GAMM
LinkDB: A0A091AR36_9GAMM
Original site: A0A091AR36_9GAMM 
ID   A0A091AR36_9GAMM        Unreviewed;       443 AA.
AC   A0A091AR36;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   16-JAN-2019, entry version 35.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:KFN41607.1};
GN   ORFNames=N790_12365 {ECO:0000313|EMBL:KFN41607.1};
OS   Arenimonas malthae CC-JY-1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1384054 {ECO:0000313|EMBL:KFN41607.1, ECO:0000313|Proteomes:UP000029392};
RN   [1] {ECO:0000313|EMBL:KFN41607.1, ECO:0000313|Proteomes:UP000029392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-JY-1 {ECO:0000313|EMBL:KFN41607.1,
RC   ECO:0000313|Proteomes:UP000029392};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas malthae.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KFN41607.1}.
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DR   EMBL; AVCH01000217; KFN41607.1; -; Genomic_DNA.
DR   RefSeq; WP_043805468.1; NZ_AVCH01000217.1.
DR   EnsemblBacteria; KFN41607; KFN41607; N790_12365.
DR   PATRIC; fig|1384054.3.peg.2759; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000029392; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   HAMAP; MF_00377; DnaA_bact; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR018312; Chromosome_initiator_DnaA_CS.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000029392};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117}.
FT   DOMAIN      140    271       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      351    420       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      302    322       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   443 AA;  49831 MW;  575EDCBA150BB5C2 CRC64;
     MDAAWPRCLE RLEAELPAEE VHTWLRPLQV ESHPDGLTLY APNEFVVDQV REHYLARIRE
     LVAHFAGSPA AVALAVGSLN RAAPARASAA PAASAGRSPA GPEFNGNLDP HYTFENFVEG
     RSNQLGRAAA LQVAQNPGKA YNPLLLYGGS GLGKTHLMYA AGNLMRQNSP GMRVMYLRSE
     QFFSAMMKSL QEKSMDQFKR QFQQVDALLI DDIQFFAGKN TTQEEFFHTF NALFDGKQQI
     ILTCDRYPRE VENLETRLKT RLTWGLSVAI EPPDFETRAA ILTAKAAERS VKLPEDVAYL
     IAKRMRSNVR DLEGALNTLA ARSNFMARPI TAEFAQETLR DLLRAQQQVV SISNIQKTVA
     DYYQLRMADL LSKRRTRSLA RPRQMAMALS KELTEHSLPE IGDAFGGRDH TTVMHACKVV
     RELREIDGKL REDWDKLLRK LSE
//
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